NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes
2012
Lee, Ae-Ree | Kim, Hee-Eun | Lee, Yeon-Mi | Jeong, Minjee | Choi, Kwang-Ho | Pak, Chin-wan | Choi, Yong-Geun | Ahn, Hee-Chul | Choi, Byong-Seok | Lee, Joon-Hwa
The Z-DNA binding domain of human ADAR1 (ZαADAR₁) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Here, we have carried out chemical shift perturbation and backbone dynamics studies of ZαADAR₁ in the free form and in complex with three DNA duplexes, d(CGCGCG)₂, d(CACGTG)₂, and d(CGTACG)₂. This study reveals that ZαADAR₁ initially binds to d(CGCGCG)₂ through the distinct conformation, especially in the unusually flexible β1–loop–α2 region, from the d(CGCGCG)₂–(ZαADAR₁)₂ complex. This study also suggests that ZαADAR₁ exhibits a distinct conformational change during the B–Z transition of non-CG-repeat DNA duplexes with low binding affinities compared to the CG-repeat DNA duplex.
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